| Literature DB >> 29278409 |
Pavel Dvorak1,2, David Bednar1,2, Pavel Vanacek1,2, Lukas Balek3, Livia Eiselleova3, Veronika Stepankova1,4,5, Eva Sebestova1,2, Michaela Kunova Bosakova3, Zaneta Konecna3, Stanislav Mazurenko1,2, Antonin Kunka1,2, Tereza Vanova3, Karolina Zoufalova3, Radka Chaloupkova1,2,4, Jan Brezovsky1,2,4, Pavel Krejci3,4, Zbynek Prokop1,2,4, Petr Dvorak3,4, Jiri Damborsky1,2,4.
Abstract
Fibroblast growth factors (FGFs) serve numerous regulatory functions in complex organisms, and their corresponding therapeutic potential is of growing interest to academics and industrial researchers alike. However, applications of these proteins are limited due to their low stability. Here we tackle this problem using a generalizable computer-assisted protein engineering strategy to create a unique modified FGF2 with nine mutations displaying unprecedented stability and uncompromised biological function. The data from the characterization of stabilized FGF2 showed a remarkable prediction potential of in silico methods and provided insight into the unfolding mechanism of the protein. The molecule holds a considerable promise for stem cell research and medical or pharmaceutical applications.Entities:
Keywords: computational design; embryonic stem cells; fibroblast growth factor; focused directed evolution; protein engineering; protein stability
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Year: 2018 PMID： 29278409 DOI： 10.1002/bit.26531
Source DB: PubMed Journal: Biotechnol Bioeng ISSN： 0006-3592 Impact factor: 4.530